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| | <StructureSection load='5fb4' size='340' side='right'caption='[[5fb4]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='5fb4' size='340' side='right'caption='[[5fb4]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fb4]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FB4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FB4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fb4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FB4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.039Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fb5|5fb5]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fb4 OCA], [http://pdbe.org/5fb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fb4 RCSB], [http://www.ebi.ac.uk/pdbsum/5fb4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fb4 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fb4 OCA], [https://pdbe.org/5fb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fb4 RCSB], [https://www.ebi.ac.uk/pdbsum/5fb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fb4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DIT9_BPPH2 DIT9_BPPH2]] Forms the distal part (knob) of the tail tube.<ref>PMID:18606992</ref> | + | [https://www.uniprot.org/uniprot/DIT9_BPPH2 DIT9_BPPH2] Forms the distal part (knob) of the tail tube.<ref>PMID:18606992</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpph2]] | + | [[Category: Bacillus virus phi29]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gui, M]] | + | [[Category: Gui M]] |
| - | [[Category: Wang, D H]] | + | [[Category: Wang DH]] |
| - | [[Category: Xiang, Y]] | + | [[Category: Xiang Y]] |
| - | [[Category: Xu, J W]] | + | [[Category: Xu JW]] |
| - | [[Category: Bacteriophage phi29]]
| + | |
| - | [[Category: Tail knob]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
DIT9_BPPH2 Forms the distal part (knob) of the tail tube.[1]
Publication Abstract from PubMed
Most bacteriophages are tailed bacteriophages with an isometric or a prolate head attached to a long contractile, long non-contractile, or short non-contractile tail. The tail is a complex machine that plays a central role in host cell recognition and attachment, cell wall and membrane penetration, and viral genome ejection. The mechanisms involved in the penetration of the inner host cell membrane by bacteriophage tails are not well understood. Here we describe structural and functional studies of the bacteriophage varphi29 tail knob protein gene product 9 (gp9). The 2.0 A crystal structure of gp9 shows that six gp9 molecules form a hexameric tube structure with six flexible hydrophobic loops blocking one end of the tube before DNA ejection. Sequence and structural analyses suggest that the loops in the tube could be membrane active. Further biochemical assays and electron microscopy structural analyses show that the six hydrophobic loops in the tube exit upon DNA ejection and form a channel that spans the lipid bilayer of the membrane and allows the release of the bacteriophage genomic DNA, suggesting that cell membrane penetration involves a pore-forming mechanism similar to that of certain non-enveloped eukaryotic viruses. A search of other phage tail proteins identified similar hydrophobic loops, which indicates that a common mechanism might be used for membrane penetration by prokaryotic viruses. These findings suggest that although prokaryotic and eukaryotic viruses use apparently very different mechanisms for infection, they have evolved similar mechanisms for breaching the cell membrane.
The bacteriophage varphi29 tail possesses a pore-forming loop for cell membrane penetration.,Xu J, Gui M, Wang D, Xiang Y Nature. 2016 Jun 15;534(7608):544-7. doi: 10.1038/nature18017. PMID:27309813[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xiang Y, Morais MC, Cohen DN, Bowman VD, Anderson DL, Rossmann MG. Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail. Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9552-7. Epub 2008 Jul 7. PMID:18606992
- ↑ Xu J, Gui M, Wang D, Xiang Y. The bacteriophage varphi29 tail possesses a pore-forming loop for cell membrane penetration. Nature. 2016 Jun 15;534(7608):544-7. doi: 10.1038/nature18017. PMID:27309813 doi:http://dx.doi.org/10.1038/nature18017
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